We plan to study, first, those physiochemical properties of proteins which depend on the secondary, tertiary or quaternary structure of the molecule, and second, to probe particular functional sites with techniques capable of resolution at the atomic level. In the first area, we are developing a technique in which proteins migrate in an inhomogeneous alternating electric field only because of their electric dipole moments analogous to the motion of proteins due to their net charge in electrophoresis. In dielectrophoresis, dipolar molecules are attracted to the region of maximum absolute electric field intensity, and at equilibrium, a concentration gradient is established which is proportional to the dipole moment. This gradient can be quantitatively measured through the change in capacitance of a suitable cell. In addition, we shall also measure the rate of build-up of decay of the gradient. We thus should obtain information on the mobility, diffusion constant, and dipole moment, as well as the dependence of these quantities on frequency. Comparison of these values for proteins with minimal primary structural differences -- for example, the substitution of one uncharged amino acid residue for another -- may elucidate the effects of primary on secondary and tertiary structure. We are applying the NMR relaxation technique to study kinetics and mechanism at the action sites of enzymes and membrane systems.